Two aspects of enzymic catalysis are to be examined: the preferred differential binding of the transition state over the reactants or products, and the utility of structural destabilization as a catalytic device. Antibodies are to be used as models for these investigations; they will be generated using transition-state-analog haptens. The consequence of preferred binding of the transition state by the antibody will be the appearance of catalytic activity for the corresponding reaction. From the binding constants and rate constants for the reaction, we will be able to characterize the thermodynamic aspects of structural destabilization. Additional research projects in bioinorganic chemistry are outlined which also capitalize on the ability to use haptens to induce the formation of antibodies with specific binding properties.